Solid-state NMR spectroscopy is one of the most commonly used techniques to study the
atomic-resolution structure and dynamics of various chemical, biological, material, and …

Magic angle spinning NMR rotating frame relaxation measurements provide a unique
experimental window into biomolecules dynamics, as is illustrated by numerous recent …

Heteronuclear correlation (HETCOR) spectroscopy is one of the key tools in the arsenal of
the solid-state NMR spectroscopist to probe chemical and spatial proximities between two …

NMR relaxation dispersion methods provide a holistic way to observe microsecond time-
scale protein backbone motion both in solution and in the solid state. Different nuclei (1H …

This review describes two rotating-frame (R 1 ρ) relaxation dispersion methods, namely the
Bloch-McConnell Relaxation Dispersion and the Near-rotary Resonance Relaxation …

Relaxation in nuclear magnetic resonance is a powerful method for obtaining spatially
resolved, timescale-specific dynamics information about molecular systems. However …

The influenza B M2 protein forms a water-filled tetrameric channel to conduct protons across
the lipid membrane. To understand how channel water mediates proton transport, we have …

Slow timescale dynamics in proteins are essential for a variety of biological functions
spanning ligand binding, enzymatic catalysis, protein folding and misfolding regulations, as …

Studying protein dynamics on microsecond‐to‐millisecond (μs‐ms) time scales can provide
important insight into protein function. In magic‐angle‐spinning (MAS) NMR, μs dynamics …

The power of chemical shift anisotropy (CSA) measurements for probing structure and
dynamics of molecules has been long recognized. NMR pulse sequences that allow …